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Structure of 3-isopropylmalate dehydrogenase

Analyse Structure of 3-isopropylmalate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OSJ
Type: protein
Length: 690 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-isopropylmalate dehydrogenase
EC: 1.1.1.85
UniProt: Q5SIY4
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3-isopropylmalate dehydrogenase (EC 1.1.1.85)	protein	345	48% helix, 21% strand	Q5SIY4

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.68	0.85	42	empty
2	594	0.67	0.77	41	empty
3	138	0.66	0.88	24	empty
4	563	0.64	0.76	48	empty
5	62	0.32	0.76	10	empty

Interfaces

1 interface between chains.

A–B · 2198 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

1OSJ · Structure of 3-isopropylmalate dehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00
Q5SIY4 · AlphaFold monomer V2.0 prediction for 3-isopropylmalate dehydrogenase (Q5SIY4) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5SIY4
Elsewhere: RCSB PDB 1OSJ · PDBe 1OSJ · UniProt Q5SIY4

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